An Abscisic Acid-Activated and Calcium-Independent Protein Kinase from Guard Cells of Fava Bean

Jiaxu Li; Sarah M. Assmann

doi:10.2307/3870474

An Abscisic Acid-Activated and Calcium-Independent Protein Kinase from Guard Cells of Fava Bean

Jiaxu Li, Sarah M. Assmann

Biology

Research output: Contribution to journal › Article › peer-review

155 Scopus citations

Abstract

Abscisic acid (ABA) regulation of stomatal aperture is known to involve both Ca²⁺-dependent and Ca²⁺-independent signal transduction pathways. Electrophysiological studies suggest that protein phosphorylation is involved in ABA action in guard cells. Using biochemical approaches, we identified an ABA-activated and Ca²⁺-independent protein kinase (AAPK) from guard cell protoplasts of fava bean. Autophosphorylation of AAPK was rapidly (∼1 min) activated by ABA in a Ca²⁺-independent manner. ABA-activated autophosphorylation of AAPK occurred on serine but not on tyrosine residues and appeared to be guard cell specific. AAPK phosphorylated histone type III-S on serine and tnreonine residues, and its activity toward histone type III-S was markedly stimulated in ABA-treated guard cell protoplasts. Our results suggest that AAPK may play an important role in the Ca²⁺-independent ABA signaling pathways of guard cells.

Original language	English (US)
Pages (from-to)	2359-2368
Number of pages	10
Journal	Plant Cell
Volume	8
Issue number	12
DOIs	https://doi.org/10.2307/3870474
State	Published - Dec 1996

All Science Journal Classification (ASJC) codes

Plant Science
Cell Biology

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title = "An Abscisic Acid-Activated and Calcium-Independent Protein Kinase from Guard Cells of Fava Bean",

abstract = "Abscisic acid (ABA) regulation of stomatal aperture is known to involve both Ca2+-dependent and Ca2+-independent signal transduction pathways. Electrophysiological studies suggest that protein phosphorylation is involved in ABA action in guard cells. Using biochemical approaches, we identified an ABA-activated and Ca2+-independent protein kinase (AAPK) from guard cell protoplasts of fava bean. Autophosphorylation of AAPK was rapidly (∼1 min) activated by ABA in a Ca2+-independent manner. ABA-activated autophosphorylation of AAPK occurred on serine but not on tyrosine residues and appeared to be guard cell specific. AAPK phosphorylated histone type III-S on serine and tnreonine residues, and its activity toward histone type III-S was markedly stimulated in ABA-treated guard cell protoplasts. Our results suggest that AAPK may play an important role in the Ca2+-independent ABA signaling pathways of guard cells.",

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T1 - An Abscisic Acid-Activated and Calcium-Independent Protein Kinase from Guard Cells of Fava Bean

AU - Li, Jiaxu

AU - Assmann, Sarah M.

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N2 - Abscisic acid (ABA) regulation of stomatal aperture is known to involve both Ca2+-dependent and Ca2+-independent signal transduction pathways. Electrophysiological studies suggest that protein phosphorylation is involved in ABA action in guard cells. Using biochemical approaches, we identified an ABA-activated and Ca2+-independent protein kinase (AAPK) from guard cell protoplasts of fava bean. Autophosphorylation of AAPK was rapidly (∼1 min) activated by ABA in a Ca2+-independent manner. ABA-activated autophosphorylation of AAPK occurred on serine but not on tyrosine residues and appeared to be guard cell specific. AAPK phosphorylated histone type III-S on serine and tnreonine residues, and its activity toward histone type III-S was markedly stimulated in ABA-treated guard cell protoplasts. Our results suggest that AAPK may play an important role in the Ca2+-independent ABA signaling pathways of guard cells.

AB - Abscisic acid (ABA) regulation of stomatal aperture is known to involve both Ca2+-dependent and Ca2+-independent signal transduction pathways. Electrophysiological studies suggest that protein phosphorylation is involved in ABA action in guard cells. Using biochemical approaches, we identified an ABA-activated and Ca2+-independent protein kinase (AAPK) from guard cell protoplasts of fava bean. Autophosphorylation of AAPK was rapidly (∼1 min) activated by ABA in a Ca2+-independent manner. ABA-activated autophosphorylation of AAPK occurred on serine but not on tyrosine residues and appeared to be guard cell specific. AAPK phosphorylated histone type III-S on serine and tnreonine residues, and its activity toward histone type III-S was markedly stimulated in ABA-treated guard cell protoplasts. Our results suggest that AAPK may play an important role in the Ca2+-independent ABA signaling pathways of guard cells.

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An Abscisic Acid-Activated and Calcium-Independent Protein Kinase from Guard Cells of Fava Bean

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